Journal
ANALYTICAL BIOCHEMISTRY
Volume 319, Issue 2, Pages 234-238Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0003-2697(03)00324-5
Keywords
calpain I; FRET; fluorescence; proteolytic activity
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Two new probes for the detection of calpain I activity based on fluorescence resonance energy transfer technology have been synthesized and evaluated. The probes incorporated the cleavage site present in alpha-spectrin, a naturally occurring substrate of calpain I. The design of the internally quenched substrates is such that the calpain-sensitive bond of the peptides (between the Tyr-Gly residues) is located centrally between the donor and the quencher chromophores. The calpain assay protocol is capable of detecting enzymatic activity in the nanomolar region. (C) 2003 Elsevier Science (USA). All rights reserved.
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